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Crystal structure of human indoleamine 2,3-dioxygenase 1 in complex with pf-06840003 in active site and si site
Analyse Crystal structure of human indoleamine 2,3-dioxygenase 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PZ1
- Type
- protein
- Length
- 753 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14902
- Ligands
- AOJ, HEM
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 376 | — | P14902 |
| B | — | protein | 377 | — | P14902 |
Ligands and binding sites
- AOJ · (3R)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione · ligand · 3 copies · chains A, B
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PZ1 · Crystal Structure of human Indoleamine 2,3-Dioxygenase 1 in complex with PF-06840003 in… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P14902
- Elsewhere: RCSB PDB 6PZ1 · PDBe 6PZ1 · UniProt P14902
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